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Q49WJ7 (PUR9_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:SSP1717
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018965

Sequences

Sequence LengthMass (Da)Tools
Q49WJ7 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 71FE36CC66337E94

FASTA49253,875
        10         20         30         40         50         60 
MKKAILSVSN KAGIVTFGQS LIEQNYELYS TGGTMRELAN GGLPVKSISE LTEFEEIMDG 

        70         80         90        100        110        120 
RVKTLHPSVH GGILADRDKP EHLEQLQAQG IDLIDMVVVN LYPFKETVAN PNVTEEDAIE 

       130        140        150        160        170        180 
NIDIGGPTML RAAAKNFKHV ITVVHPADYN EVIDKLKNGT LDEAYRKSLM IKVFEHTNEY 

       190        200        210        220        230        240 
DAAIVDYFKD NKESLRYGEN PQQSAYFVRT SDAKHTLAGA KQLHGKQLSY NNIKDADAAL 

       250        260        270        280        290        300 
SLVKQFEQPA AVAVKHMNPC GVGVAETIDE AYKHAFDADN QSIFGGIVAL NRTVEKSLAE 

       310        320        330        340        350        360 
VLHGIFLEVV IAPKFTQEAL EVLGKKKNIR LLEIDMTIDN SEQELVSVSG GYLVQDKDNV 

       370        380        390        400        410        420 
KLNREDMTVV TEVEPTEAQW DAMLLGWKVV ASVKSNAVIL SNAKQTVGIG AGQMNRVGSA 

       430        440        450        460        470        480 
QIAIERAIEI NDDVAMVSDG FFPMDDTVEL AANSGIKAII QPGGSIKDQE SIDMANKHGI 

       490 
AMVTTGVRHF KH 

« Hide

References

[1]"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15305 / DSM 20229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008934 Genomic DNA. Translation: BAE18862.1.
RefSeqYP_301807.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ49WJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342451.SSP1717.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE18862; BAE18862; SSP1717.
GeneID3616626.
KEGGssp:SSP1717.
PATRIC19625021. VBIStaSap90642_1716.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycSSAP342451:GKFA-1777-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_STAS1
AccessionPrimary (citable) accession number: Q49WJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways